2gs4

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(New page: 200px<br /><applet load="2gs4" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gs4, resolution 2.00&Aring;" /> '''The crystal structur...)
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[[Image:2gs4.gif|left|200px]]<br /><applet load="2gs4" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2gs4, resolution 2.00&Aring;" />
caption="2gs4, resolution 2.00&Aring;" />
'''The crystal structure of the E.coli stress protein YciF.'''<br />
'''The crystal structure of the E.coli stress protein YciF.'''<br />
==Overview==
==Overview==
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YciF is a protein that is up-regulated when bacteria experience stress, conditions, and is highly conserved in a range of bacterial species. YciF, has no known structure or biochemical function. To learn more about its, potential molecular function and its role in the bacterial stress, response, we solved the crystal structure of YciF at 2.0 Angstrom, resolution by the multiple wavelength anomalous diffraction (MAD), technique. YciF is a dimer in solution, and forms a homodimer in the, crystal asymmetric unit. The two monomers form a dimer with a molecular, twofold axis, with a significant burial of solvent-accessible surface, area. The protein is an all-alpha protein composed of five helices: a, four-helix bundle, and a short additional helix at the dimer interface., The protein is structurally similar to portions of the diiron-containing, proteins, rubrerythrin and the Bacillus anthracis Dlp-2.
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YciF is a protein that is up-regulated when bacteria experience stress conditions, and is highly conserved in a range of bacterial species. YciF has no known structure or biochemical function. To learn more about its potential molecular function and its role in the bacterial stress response, we solved the crystal structure of YciF at 2.0 Angstrom resolution by the multiple wavelength anomalous diffraction (MAD) technique. YciF is a dimer in solution, and forms a homodimer in the crystal asymmetric unit. The two monomers form a dimer with a molecular twofold axis, with a significant burial of solvent-accessible surface area. The protein is an all-alpha protein composed of five helices: a four-helix bundle, and a short additional helix at the dimer interface. The protein is structurally similar to portions of the diiron-containing proteins, rubrerythrin and the Bacillus anthracis Dlp-2.
==About this Structure==
==About this Structure==
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2GS4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2GS4 OCA].
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2GS4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GS4 OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Bellamy, H.D.]]
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[[Category: Bellamy, H D.]]
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[[Category: Fox, R.O.]]
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[[Category: Fox, R O.]]
[[Category: Hindupur, A.]]
[[Category: Hindupur, A.]]
[[Category: Liu, D.]]
[[Category: Liu, D.]]
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[[Category: White, M.A.]]
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[[Category: White, M A.]]
[[Category: Zhao, Y.]]
[[Category: Zhao, Y.]]
[[Category: rubrerythrin]]
[[Category: rubrerythrin]]
[[Category: stress proteins]]
[[Category: stress proteins]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:21:49 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:34:45 2008''

Revision as of 15:34, 21 February 2008


2gs4, resolution 2.00Å

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The crystal structure of the E.coli stress protein YciF.

Overview

YciF is a protein that is up-regulated when bacteria experience stress conditions, and is highly conserved in a range of bacterial species. YciF has no known structure or biochemical function. To learn more about its potential molecular function and its role in the bacterial stress response, we solved the crystal structure of YciF at 2.0 Angstrom resolution by the multiple wavelength anomalous diffraction (MAD) technique. YciF is a dimer in solution, and forms a homodimer in the crystal asymmetric unit. The two monomers form a dimer with a molecular twofold axis, with a significant burial of solvent-accessible surface area. The protein is an all-alpha protein composed of five helices: a four-helix bundle, and a short additional helix at the dimer interface. The protein is structurally similar to portions of the diiron-containing proteins, rubrerythrin and the Bacillus anthracis Dlp-2.

About this Structure

2GS4 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

The crystal structure of the E. coli stress protein YciF., Hindupur A, Liu D, Zhao Y, Bellamy HD, White MA, Fox RO, Protein Sci. 2006 Nov;15(11):2605-11. Epub 2006 Sep 25. PMID:17001035

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